ID D8LUX0_BLAHO Unreviewed; 486 AA.
AC D8LUX0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN ORFNames=GSBLH_T00000063001 {ECO:0000313|EMBL:CBK19609.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK19609.2};
RN [1] {ECO:0000313|EMBL:CBK19609.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK19609.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000256|RuleBase:RU000585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000256|RuleBase:RU000585};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000412-50, ECO:0000256|RuleBase:RU000585};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU000585}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC ECO:0000256|RuleBase:RU000585}.
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DR EMBL; FN668638; CBK19609.2; -; Genomic_DNA.
DR RefSeq; XP_012893657.1; XM_013038203.1.
DR AlphaFoldDB; D8LUX0; -.
DR EnsemblProtists; CBK19609; CBK19609; GSBLH_T00000063001.
DR GeneID; 24917385; -.
DR InParanoid; D8LUX0; -.
DR OrthoDB; 5358603at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000008312; Unassembled WGS sequence.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR11680:SF35; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:CBK19609.2};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000585};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000412-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000008312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 33..425
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 486 AA; 53735 MW; 71213700484849F9 CRC64;
MISALSRSIR LSAARITPVA RAGFATIPGR VPLEEHDPEL FDLIEKEKNR SWKSLEMIAS
ENFTSRAVME CLGSCLTNKY SEGYPGHRYY GGNEYIDQIE ELCKKRALAA YHLDPEKWGV
NVQPYSGSPC NLAVYTGLLK PGSRMMGLDL PSGGHLTHGY YTYNAKTHTR KALSGSSIFF
ETLPYHVDPK TGLVDYDFME QIAGIYRPQM IICGASAYPR EWDYARIRKV ADASGAIMMM
DMAHISGLVA TGEAANPFEY CDVVTTTTHK SLRGPRAGMI FFRKDERDFE RKINDAVFPG
LQGGPHDHQI AAIATQLKEV ASPEFKEYCV QVKKNAKALA QALMDMGYTI CTNGTDNHLL
LWDVRPLGLT GSKIEKVCDL INISLNKNTV HGDKSAQSPG GVRIGTPALT TRGLKEADFK
KVAGFLDRAV KISLDVQKSS GKKLKDFVAA LPNNKDIPVL AHEVAQFATS FPMPGFDTET
MRYKNL
//